id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
work_luaxo5mksvaqzoiflczn7iakxu	Jose L. Nieva	Fusogenic Activity of the HIV-1 Gp41 MPER-TMD Region: Mechanism and Targeting by Immunogens and Inhibitors	2013	1	.pdf	application/pdf	1533	93	44	HIV Fusion Peptide Perturbs Membrane Structure in a Cholesterol HIV-1 membrane fusion is mediated by sequential binding of the viral homotrimeric Env (gp120/gp41) to cellular CD4 and chemokine receptor (CXCR4 or bridges the viral and cellular membranes, and exposes the N-HR and C-HR domains which are targeted by HIV-1 fusion inhibitors T20 and 5-Helix, respectively. Evolution of HIV-1 Resistance to a Cholesterol-Linked D-Peptide Fusion Viral propagation in increasing inhibitor concentrations produced HIV-1 populations with 50to 100-fold reduced sensitivity cholPIE12-trimer. HIV Fusion Peptide Perturbs Membrane Structure in a Cholesterol Dependent Fashion CD4 Binding Induces an Asymmetric Transition of HIV-1 Env from its Native Conformation into the Prehairpin Intermediate State Evolution of HIV-1 Resistance to a Cholesterol-Linked D-Peptide Fusion Inhibitor Fusogenic Activity of the HIV-1 Gp41 MPER-TMD Region: Mechanism and Targeting by Immunogens and Inhibitors Fusogenic Activity of the HIV-1 Gp41 MPER-TMD Region: Mechanism and Targeting by Immunogens and Inhibitors	./cache/work_luaxo5mksvaqzoiflczn7iakxu.pdf	./txt/work_luaxo5mksvaqzoiflczn7iakxu.txt